Histidinol-phosphate aminotransferase
Details
- Name
- Histidinol-phosphate aminotransferase
- Synonyms
- 2.6.1.9
- HPAT
- HspAT
- Imidazole acetol-phosphate transaminase
- Gene Name
- hisC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010979|Histidinol-phosphate aminotransferase MSTVTITDLARENVRNLTPYQSARRLGGNGDVWLNANEYPTAVEFQLTQQTLNRYPECQP KAVIENYAQYAGVKPEQVLVSRGADEGIELLIRAFCEPGKDAILYCPPTYGMYSVSAETI GVECRTVPTLDNWQLDLQGISDKLDGVKVVYVCSPNNPTGQLINPQDFRTLLELTRGKAI VVADEAYIEFCPQASLAGWLAEYPHLAILRTLSKAFALAGLRCGFTLANEEVINLLMKVI APYPLSTPVADIAAQALSPQGIVAMRERVAQIIAEREYLIAALKEIPCVEQVFDSETNYI LARFKASSAVFKSLWDQGIILRDQNKQPSLSGCLRITVGTREESQRVIDALRAEQV
- Number of residues
- 356
- Molecular Weight
- 39359.715
- Theoretical pI
- 4.72
- GO Classification
- Functionshistidinol-phosphate transaminase activity / identical protein binding / L-phenylalanine / pyridoxal phosphate bindingProcesseshistidine biosynthetic processComponentscytosol
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Pfam Domain Function
- Aminotran_1_2 (PF00155)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0010980|Histidinol-phosphate aminotransferase (hisC) ATGAGCACCGTGACTATTACCGATTTAGCGCGTGAAAACGTCCGCAACCTGACGCCGTAT CAGTCGGCGCGTCGTCTGGGCGGTAACGGCGATGTCTGGCTGAACGCCAACGAATACCCC ACTGCCGTGGAGTTTCAGCTTACTCAGCAAACGCTCAACCGCTACCCGGAATGCCAGCCG AAAGCGGTGATTGAAAATTACGCGCAATATGCAGGCGTAAAACCGGAGCAGGTGCTGGTC AGCCGTGGCGCGGACGAAGGTATTGAACTGCTGATTCGCGCTTTTTGCGAACCGGGTAAA GACGCCATCCTCTACTGCCCGCCAACGTACGGCATGTACAGCGTCAGCGCCGAAACGATT GGCGTCGAGTGCCGCACAGTGCCGACGCTGGACAACTGGCAACTGGACTTACAGGGCATT TCCGACAAGCTGGACGGCGTAAAAGTGGTTTATGTTTGCAGCCCCAATAACCCGACCGGG CAACTGATCAATCCGCAGGATTTTCGCACCCTGCTGGAGTTAACCCGCGGTAAGGCGATT GTGGTTGCCGATGAAGCCTATATCGAGTTTTGCCCGCAGGCATCGCTGGCTGGCTGGCTG GCGGAATATCCGCACCTGGCTATTTTACGCACACTGTCGAAAGCTTTTGCTCTGGCGGGG CTTCGTTGCGGATTTACGCTGGCAAACGAAGAAGTCATCAACCTGCTGATGAAAGTGATC GCCCCCTACCCGCTCTCGACGCCGGTTGCCGACATTGCGGCCCAGGCGTTAAGCCCACAG GGAATCGTCGCCATGCGCGAACGGGTAGCGCAAATTATTGCAGAACGCGAATACCTGATT GCCGCACTGAAAGAGATCCCCTGCGTAGAGCAGGTTTTCGACTCTGAAACCAACTACATT CTGGCGCGCTTTAAAGCCTCCAGTGCGGTGTTTAAATCTTTGTGGGATCAGGGCATTATC TTACGTGATCAGAATAAACAACCCTCTTTAAGCGGCTGCCTGCGAATTACCGTCGGAACC CGTGAAGAAAGCCAGCGCGTCATTGACGCCTTACGTGCGGAGCAAGTTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P06986 UniProtKB Entry Name HIS8_ECOLI GenBank Protein ID 41695 GenBank Gene ID X03416 - General References
- Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB: Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J Mol Biol. 1988 Oct 5;203(3):585-606. [Article]
- Grisolia V, Carlomagno MS, Nappo AG, Bruni CB: Cloning, structure, and expression of the Escherichia coli K-12 hisC gene. J Bacteriol. 1985 Dec;164(3):1317-23. [Article]
- Jovanovic G, Kostic T, Jankovic M, Savic DJ: Nucleotide sequence of the Escherichia coli K12 histidine operon revisited. J Mol Biol. 1994 Jun 10;239(3):433-5. [Article]
- Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A: Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. J Mol Biol. 2001 Aug 24;311(4):761-76. [Article]
- Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H: Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Biochemistry. 2001 Apr 17;40(15):4633-44. [Article]